Vimentin mediates uptake of C3 exoenzyme.
Vimentin mediates uptake of C3 exoenzyme.
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DOI：
10.1371/journal.pone.0101071
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发表时间：
2014
期刊：
影响因子：
3.7
通讯作者：
Just I
中科院分区：
文献类型：
--
作者：
Rohrbeck A;Schröder A;Hagemann S;Pich A;Höltje M;Ahnert-Hilger G;Just I
肉毒梭菌C3外切酶（C3）通过ADP-核糖基化选择性灭活RhoA/B/C GTP酶。基于这种底物特异性，C3是细胞生物学中公认的工具。C3被真核细胞摄取，尽管缺乏摄取和转运结构域。基于不同的方法，波形蛋白通过质谱被鉴定为膜C3相互作用伴侣。事实上，波形蛋白部分定位于海马HT 22细胞和J744A.1巨噬细胞的外表面。结构域分析确定杆结构域为C3的结合伴侣。波形蛋白还参与C3的摄取，如通过波形蛋白在HT 22和J774A.1细胞中的敲低所示。波形蛋白干扰剂丙烯酰胺阻断C3摄取的发现进一步支持了波形蛋白参与C3摄取。波形蛋白不仅是中间丝网络的主要组织元件，而且还参与C3外切酶的结合和摄取。
Clostridium botulinum C3 exoenzyme (C3) selectively inactivates RhoA/B/C GTPases by ADP-ribosylation. Based on this substrate specificity C3 is a well-established tool in cell biology. C3 is taken up by eukaryotic cells although lacking an uptake and translocation domain. Based on different approaches vimentin was identified as membranous C3-interaction partner by mass spectrometry. Vimentin in fact was partly localized at the outer surface of hippocampal HT22 cells and J744A.1 macrophages. Domain analysis identified the rod domain as binding partner of C3. Vimentin was also involved in uptake of C3 as shown by knock down of vimentin in HT22 and J774A.1 cells. The involvement of vimentin in uptake of C3 was further supported by the findings that the vimentin disruptor acrylamide blocked uptake of C3. Vimentin is not only a major organizing element of the intermediate filament network but is also involved in both binding and uptake of C3 exoenzyme.
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影响因子：
3.4
作者：
Fahrer, Joerg;Kuban, Jasmin;Barth, Holger
通讯作者：
Barth, Holger
DOI：
10.1083/jcb.134.4.971
发表时间：
1996-08
期刊：
The Journal of cell biology
影响因子：
--
作者：
Goldman RD;Khuon S;Chou YH;Opal P;Steinert PM
通讯作者：
Steinert PM
影响因子：
5
作者：
Das, Soma;Ravi, Vasanthapuram;Desai, Anita
通讯作者：
Desai, Anita
影响因子：
3.8
作者：
Auer, Maria;Allodi, Ilary;Klimaschewski, Lars
通讯作者：
Klimaschewski, Lars
影响因子：
5.3
作者：
Auer M;Schweigreiter R;Hausott B;Thongrong S;Höltje M;Just I;Bandtlow C;Klimaschewski L
通讯作者：
Klimaschewski L